Corticosteroid Binder IB, A Potential Second Glucocorticoid Receptor

  • Gerald Litwack
  • Michael Mayer
  • Virginia Ohl
  • Bernard Sekula
Conference paper


In 1973 (Litwack et al. 1973) we discovered a second liver glucocorticoid binding protein separable from transcortin and from the glucocorticoid receptor that we named binder II. We named the new protein IB. The nomenclature developed from the sequence of elution of glucocorticoid or metabolite binding proteins from DEAE—Sephadex columns at pH 7.5. Since ligandin, a steroid metabolite binding protein eluted first (pI ~8.9), it was named IA and the new binding protein was eluted just after it, hence IB. The receptor eluted next (II) and subsequently other proteins including Transcortin (IV) were eluted. Initially we thought, since IB was a binder of unmetabolized potent glucocorticoids, it might function as a “storage” protein in the cytosol, perhaps analogously to the cytosolic thyroid hormone binding protein or that it might be a second receptor (Litwack and Rosenfield 1975). Recently, there has been much emphasis on the proteolytic degradation of the glucocorticoid receptor into forms that retain the steroid-binding function and either retain or do not retain the DNA-binding site (Wrange and Gustafsson 1978; Sherman et al. 1979). In this paper we review and extend the information on corticosteroid binder IB. We try to draw some conclusions about its possible function in light of the recent emphasis on artifactual proteolytic digestion products of the glucocorticoid receptor.


Glucocorticoid Receptor Triamcinolone Acetonide Liver Cytosol Chloromethyl Ketone Proteolytic Inhibitor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Blobel G, Potter VR (1966) Science 154: 1662–1665PubMedCrossRefGoogle Scholar
  2. Carlstedt-Duke J, Wrange Ö, Dahlberg E, Gustafsson J-A, Högberg B (1979) J Biol Chem 254: 1537–1539PubMedGoogle Scholar
  3. Dolan KP, Diaz-Gil JJ, Litwack G (1980) Arch Biochem Biophys 201: 476–485PubMedCrossRefGoogle Scholar
  4. Eisen HJ (1980) Proc Nat Acad Sci 77: 3893–3897PubMedCrossRefGoogle Scholar
  5. Eisen HJ, Schleenbaker RE, Simons Jr SS (1981) J Biol Chem 256: 12920–12925PubMedGoogle Scholar
  6. Litwack G, Filler R, Rosenfield SA, Lichtash N, Singer S (1973) J Biol Chem 55: 977–984Google Scholar
  7. Litwack G, Rosenfield SA (1975) J Biol Chem 215: 6799–6805Google Scholar
  8. Marković RD, Eisen HJ, Parchman LG, Barnett CA, Litwack G (1980) Biochemistry 19: 4556–4564PubMedCrossRefGoogle Scholar
  9. Marković RD, Litwack G (1980) Arch Biochem Biophys 202: 374–379PubMedCrossRefGoogle Scholar
  10. Munck A, Foley R (1979) Nature 278: 752–753PubMedCrossRefGoogle Scholar
  11. Parchman LG, Litwack G (1977) Arch Biochem Biophys 183: 374–382PubMedCrossRefGoogle Scholar
  12. Sherman MR, Barzilai D, Pine PR, Tuazon, FB (1979) In: Leavitt WW, Clark JH (eds) Steroid Hormone Receptor Systems, Plenum Press, New York and London, pp 357–375Google Scholar
  13. Stevens J, Stevens YW (1981a) Cancer Res 41: 125–133PubMedGoogle Scholar
  14. Stevens J, Eisen HJ, Stevens YW, Haubenstock H, Rosenthal RL, Artishevsky A (1981b) Cancer Res 41: 134–137PubMedGoogle Scholar
  15. Wrange Ö, Gustafsson J-A (1978) J Biol Chem 253: 856–865PubMedGoogle Scholar

Copyright information

© Springer-Verlag New York Inc. 1983

Authors and Affiliations

  • Gerald Litwack
  • Michael Mayer
  • Virginia Ohl
  • Bernard Sekula

There are no affiliations available

Personalised recommendations